Function of a newly synthesized protein depends on their three-dimensional confirmations. The cells utilize its evolutionary conserved machinery to maintain the protein quality. Protein quality control plays an important role at the cellular level in the removal of misfolded and aggregated proteins. The folding mechanism is mainly assisted by molecular chaperones, which are generally heat shock proteins. Dysregulation of these mechanism leads to the pathogenesis of number of diseases, such as cystic fibrosis and neurodegenerative disease. Cystic fibrosis transmembrane conductance regulator (CFTR) is one of the challenged proteins with number of misfolding defects, which leads to the variety of severity in the patients. Approximately 2000 mutations evidenced in the CF gene, out of which ~120 are recognized to be CF causing mutations. Our aim is to elucidate the proper folding and trafficking of CFTR to the apical membrane of the epithelial cells.